TORT_ECOLI
ID TORT_ECOLI Reviewed; 342 AA.
AC P38683; P75888;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Periplasmic protein TorT;
DE Flags: Precursor;
GN Name=torT; Synonyms=yccH; OrderedLocusNames=b0994, JW0979;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=8083154; DOI=10.1128/jb.176.18.5601-5606.1994;
RA Simon G., Mejean V., Jourlin C., Chippaux M., Pascal M.-C.;
RT "The torR gene of Escherichia coli encodes a response regulator protein
RT involved in the expression of the trimethylamine N-oxide reductase genes.";
RL J. Bacteriol. 176:5601-5606(1994).
RN [2]
RP PROTEIN SEQUENCE OF 19-24, SEQUENCE REVISION TO 29-30, AND
RP CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=8576063; DOI=10.1128/jb.178.4.1219-1223.1996;
RA Jourlin C., Simon G., Pommier J., Chippaux M., Mejean V.;
RT "The periplasmic TorT protein is required for trimethylamine N-oxide
RT reductase gene induction in Escherichia coli.";
RL J. Bacteriol. 178:1219-1223(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Upon binding a putative inducer it probably interacts with
CC TorS and allows it to play a role in the induction of the torCAD operon
CC for trimethylamine N-oxide reductase.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; X94231; CAA63921.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74079.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36136.1; -; Genomic_DNA.
DR PIR; H64840; H64840.
DR RefSeq; NP_415514.1; NC_000913.3.
DR RefSeq; WP_001264933.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P38683; -.
DR SMR; P38683; -.
DR BioGRID; 4262840; 338.
DR STRING; 511145.b0994; -.
DR PaxDb; P38683; -.
DR PRIDE; P38683; -.
DR EnsemblBacteria; AAC74079; AAC74079; b0994.
DR EnsemblBacteria; BAA36136; BAA36136; BAA36136.
DR GeneID; 66670728; -.
DR GeneID; 946289; -.
DR KEGG; ecj:JW0979; -.
DR KEGG; eco:b0994; -.
DR PATRIC; fig|1411691.4.peg.1277; -.
DR EchoBASE; EB2500; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_053104_0_0_6; -.
DR OMA; ISQIEDC; -.
DR PhylomeDB; P38683; -.
DR BioCyc; EcoCyc:TORT-MON; -.
DR PRO; PR:P38683; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR InterPro; IPR001761; Peripla_BP/Lac1_sug-bd_dom.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR014301; TMAO_TorT.
DR Pfam; PF00532; Peripla_BP_1; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR TIGRFAMs; TIGR02955; TMAO_TorT; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:8576063"
FT CHAIN 19..342
FT /note="Periplasmic protein TorT"
FT /id="PRO_0000031736"
FT CONFLICT 59
FT /note="W -> S (in Ref. 1; CAA63921)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="A -> R (in Ref. 1; CAA63921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 37865 MW; 82FC7AAEDF3B2DB9 CRC64;
MRVLLFLLLS LFMLPAFSAD NLLRWHDAQH FTVQASTPLK AKRAWKLCAL YPSLKDSYWL
SLNYGMQEAA RRYGVDLKVL EAGGYSQLAT QQAQIDQCKQ WGAEAILLGS STTSFPDLQK
QVASLPVIEL VNAIDAPQVK SRVGVPWFQM GYQPGRYLVQ WAHGKPLNVL LMPGPDNAGG
SKEMVEGFRA AIAGSPVRIV DIALGDNDIE IQRNLLQEML ERHPEIDVVA GTAIAAEAAM
GEGRNLKTPL TVVSFYLSHQ VYRGLKRGRV IMAASDQMVW QGELAVEQAI RQLQGQSVSD
NVSPPILVLT PKNADREHIR RSLSPGGFRP VYFYQHTSAA KK
